Reviewed, UniProtKB/Swiss-Prot Q9EQS0 (TALDO_RAT)

Names and origin

Protein names

Recommended name:
    Transaldolase
    EC=2.2.1.2

Gene names

Name:

Taldo1

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	337 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway By similarity.
Catalytic activity	Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate.
Pathway	Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the transaldolase family. Type 1 subfamily.

Ontologies

Keywords
Biological process	Pentose shunt
Cellular component	Cytoplasm
Molecular function	Transferase
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	fructose 6-phosphate metabolic process Inferred from direct assay. Source: RGD glyceraldehyde-3-phosphate metabolic process Inferred from direct assay. Source: RGD pentose-phosphate shunt, non-oxidative branch Inferred from direct assay. Source: RGD
Cellular component	cytosol Inferred from direct assay. Source: RGD microsome Inferred from direct assay. Source: RGD soluble fraction Inferred from direct assay. Source: RGD
Molecular function	monosaccharide binding Inferred from direct assay. Source: RGD transaldolase activity Inferred from direct assay. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 337	337	Transaldolase		PRO_0000173567
Sites
	Active site	142	1	By similarity
Amino acid modifications
	Modified residue	4	1	Phosphoserine By similarity
	Modified residue	219	1	N6-acetyllysine By similarity
	Modified residue	237	1	Phosphoserine Ref.4
	Modified residue	269	1	N6-acetyllysine By similarity
	Modified residue	286	1	N6-acetyllysine By similarity
	Modified residue	321	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	100	1	P → L in AAG43169. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9EQS0-1 [UniParc]. Last modified April 4, 2006. Version 2. Checksum: F01F64276053B45D	FASTA	337	37,460
	10 20 30 40 50 60 MSGSPVKRQR MESALDQLKQ FTTVVADTGD FNAIDEYKPQ DATTNPSLIL AAAQMPAYQE 70 80 90 100 110 120 LVEEAIAYGK KLGGPQEEQI KNAIDKLFVL FGAEILKKIP GRVSTEVDAR LSFDKDAMVA 130 140 150 160 170 180 RARRIIELYK EAGISKDRIL IKLSSTWEGI QAGKELEEQH GIHCNMTLLF SFAQAVACAE 190 200 210 220 230 240 AGVTLISPFV GRILDWHVAN TDKKSYEPQE DPGVKSVTKI YNYYKKFGYK TIVMGASFRN 250 260 270 280 290 300 TGEIKALAGC DFLTISPKLL GELLKDSSKL APTLSVKAAQ TSDLEKIHLD EKAFRWLHNE 310 320 330 DQMAVEKLSD GIRKFAADAI KLERMLTERM FSAENGK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Perl A., Bachand G. Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pituitary.
[3]	Lubec G., Chen W.-Q., Kang S.U. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 72-81; 103-121; 125-130; 220-225; 246-265; 270-277 AND 315-321, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Brain and Hippocampus.
[4]	"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS." Moser K., White F.M. J. Proteome Res. 5:98-104(2006) [PubMed: 16396499] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF069306 mRNA. Translation: AAG43169.1. BC059126 mRNA. Translation: AAH59126.1.
IPI	IPI00190377.
RefSeq	NP_113999.2.
UniGene	Rn.3136
3D structure databases
HSSP	HSSP built from PDB template 1F05 based on UniProtKB P37837.
SMR	Q9EQS0. Positions 13-331.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9EQS0.
PTM databases
PhosphoSite	Q9EQS0.
Proteomic databases
PRIDE	Q9EQS0.
Genome annotation databases
Ensembl	ENSRNOT00000024863; ENSRNOP00000024863; ENSRNOG00000018367; Rattus norvegicus. [Genome view]
GeneID	83688.
KEGG	rno:83688.
NMPDR	fig|10116.3.peg.3280.
UCSC	NM_031811. rat.
Organism-specific databases
CTD	83688.
RGD	620674. Taldo1.
Phylogenomic databases
HOVERGEN	Q9EQS0.
OMA	EYKPQDA.
Enzyme and pathway databases
BRENDA	2.2.1.2. 248.
Gene expression databases
ArrayExpress	Q9EQS0.
Genevestigator	Q9EQS0.
GermOnline	ENSRNOG00000018367. Rattus norvegicus.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR001585. Transaldolase. IPR004730. Transaldolase_AB. IPR018225. Transaldolase_AS. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHER	PTHR10683. Transaldolase. 1 hit. PTHR10683:SF3. Transaldolase_AB. 1 hit.
Pfam	PF00923. Transaldolase. 1 hit. [Graphical view]
TIGRFAMs	TIGR00874. talAB. 1 hit.
PROSITE	PS01054. TRANSALDOLASE_1. 1 hit. PS00958. TRANSALDOLASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	616261.

Entry information

Entry name

TALDO_RAT

Accession

Primary (citable) accession number: Q9EQS0
Secondary accession number(s): Q6PCV1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 5, 2001
Last sequence update:	April 4, 2006
Last modified:	November 3, 2009
This is version 65 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)